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PubMed1998

A novel bacteriocin with a YGNGV motif from vegetable-associated Enterococcus mundtii: full characterization and interaction with target organisms.

A novel broad-spectrum antimicrobial peptide produced by vegetable-associated Enterococcus mundtii was purified and characterized, and designated mundticin. To our knowledge, this is the first report on bacteriocin production by this organism. The elucidation of the full primary amino acid sequence of mundticin (KYYGNGVSCNKKGCSVDWGKAIGIIGNNSAANLATGGAAGWSK) revealed that this antimicrobial peptide belongs to the class IIa bacteriocins of lactic acid bacteria which share a highly conserved N-terminal 'YGNGV' motif. Data obtained by computer modelling indicated an oblique orientation of the alpha-helical regions of mundticin and homologous class IIa bacteriocins at a hydrophobic-hydrophilic interface, which may play a role in the destabilization of phospholipid bilayers. The average mass of mundticin, as determined by electron spray mass spectrometry, was found to be 4287.21+/-0.59 Da. With respect to its biological activity, mundticin was shown to inhibit the growth of Listeria monocytogenes, Clostridium botulinum and a variety of lactic acid bacteria. Moreover, it was demonstrated to have a bactericidal effect on L. monocytogenes as a result of the dissipation of the membrane potential, and a loss of intracellular ATP in absence of ATP leakage. Its good solubility in water, and its stability over a wide pH and temperature range indicate the potential of this broad spectrum bacteriocin as a natural preservation agent for foods.

Amino Acid Sequence↗
PubMed2002

Biochemical characterisation and genetic analysis of aureocin A53, a new, atypical bacteriocin from Staphylococcus aureus.

Aureocin A53 is produced by Staphylococcus aureus A53. It is encoded on a 10.4 kb plasmid, pRJ9, and is active against Listeria monocytogenes. Aureocin A53 is a highly cationic 51-residue peptide containing ten lysine and five tryptophan residues. Aureocin A53 was purified to homogeneity by hydrophobic-interaction, cation-exchange, and reverse-phase chromatography. MALDI-TOF mass spectrometry yielded a molecular mass of 6012.5 Da, which was 28 Da higher than predicted from the structural gene sequence of the bacteriocin. The mass increment resulted from an N-formylmethionine residue, indicating that the aureocin A53 is synthesised and secreted without a typical bacteriocin leader sequence or sec-dependent signal peptide. The structural identity of aureocin A53 was verified by Edman sequencing after de-blocking with cyanogen bromide and extensive mass spectrometry analysis of enzymatically and laser-generated fragments. The complete sequence of pRJ9 was determined and none of the open reading frames identified in the vicinity of the structural gene aucA showed similarity to genes that are typically found in bacteriocin gene clusters. Thus, neither a dedicated protease or transporter, nor modifying enzymes and regulatory elements seemed to be involved in the production of aureocin A53. Further unique features that distinguish aureocin A53 from other peptide bacteriocins include remarkable protease stability and a defined, rigid structure in aqueous solution.

Amino Acid Sequence↗
PubMed2000

A gene cluster encoding plantaricin 1.25beta and other bacteriocin-like peptides in Lactobacillus plantarum TMW1.25.

Plantaricin 1.25beta is a thermostable class two bacteriocin produced by Lactobacillus plantarum TMW1.25 isolated from sausage fermentation. It is co-produced with several other bacteriocin-like peptides. Using oligonucleotides derived from previously determined peptide sequences, a 3.8 kb DNA fragment could be amplified. A neighboring 1.8 kb fragment was amplified using ligation-anchored single-specific-primer PCR. Sequencing of the complete 5.6 kb stretch revealed that the structural gene for plantaricin 1.25beta, plnB, was located downstream of another bacteriocin gene, plnC. Seven other open reading frames were detected, including plnK encoding a bacteriocin-like peptide, but not including any putative immunity genes. Interestingly, the gene cluster contained an IS30-like insertion sequence, designated IS125, as well as an ISS1 homolog.

Amino Acid Sequence↗
PubMed2000

Cloning and expression of the genes involved in the production of and immunity against the bacteriocin lacticin RM.

The production of lacticin RM, a novel bacteriocin produced by Lactococcus lactis subsp. lactis EZ26, is associated with the presence of a 6-kb plasmid, pHU1. The information necessary for lacticin RM production and immunity was localized to a 2.5-kb SalI-Eco47III fragment. Sequencing analysis of this fragment revealed the presence of six open reading frames (ORFs). Deletion and mutation analyses showed that orfX and orfY are not required for lacticin RM production or immunity, whereas the other ORFs (lacA, lacF, lacG and lacI) are necessary for the bacteriocin's production. Transcription analysis indicated that lacA, lacF and lacG are organized in an operon. lacA is probably the lacticin RM structural gene. It putatively encodes a 134-amino acid peptide, and it does not share homology with known bacteriocins. The deduced LacG protein is hydrophobic and consists of six potential trans-membrane helices. lacF encodes a conserved ATP-binding domain homologous to ABC transporters known in bacteriocin immunity systems. LacF and LacG may form an active ABC transporter. Gene-disruption mutations indicated that both are required for immunity against lacticin RM. lacI encodes a small cationic protein, which is required for the production of and immunity to lacticin RM. Protection was obtained only when lacF, lacG and lacI were present together.

ATP-Binding Cassette Transporters↗
PubMed2001

Detection and preliminary characterization of a bacteriocin (plantaricin 35d) produced by a Lactobacillus plantarum strain.

Lactic acid bacteria (134) from Italian sausages were tested for the production of antimicrobial substances (bacteriocins). Six percent of these showed antibacterial activity against one or several closely related microorganisms used as indicators. Lactobacillus plantarum 35d in particular produced a bacteriocin of high activity (320 AU ml(-1)) and a wide range of antimicrobial activity including S. aureus, L. monocytogenes, and A. hydrophila. The bacteriocin withstood heating at 80 degrees C for 120 min and storage at 4 degrees C for 6 months. The mode of action was identified as bactericidal. The apparent molecular weight of the bacteriocin extracted with n-butanol was estimated to be 4.5 kDa.

Animals↗
PubMed2001

Mode of action, purification and amino acid sequence of plantaricin C19, an anti-Listeria bacteriocin produced by Lactobacillus plantarum C19.

Plantaricin C19, an anti-Listeria bacteriocin, was successfully purified by adsorption to and release from producing cells at low pH combined with reverse phase high-performance liquid chromatography (HPLC). The purification resulted in a 900-fold increase in specific activity with a yield of 15% of the original activity. Mass spectrometry analysis gave a molecular weight of 3845.3. Protein microsequencing identified 36 amino acids. Plantaricin C19 is rich in both hydrophobic and basic amino acids in good accordance with its basic and hydrophobic character. Comparison of the amino acid sequence of plantaricin C19, with the sequence of some other anti-Listeria bacteriocins produced with lactic acid bacteria, revealed that plantaricin C19 has in its N-terminal region the consensus sequence--YYGNGL--(uniquely with Valine instead of Leucine as found in all other bacteriocins), identifying plantaricin C19 as a pediocin-like bacteriocin. Plantaricin C19 exerted a bacteriostatic action on sensitive cells of Listeria grayi IP 6818 in BHI broth. No loss of intracellular K+, Mg2+ or UV-absorbing materials was observed. Adsorption of plantaricin C19 on L. grayi CIP 6818 decreased in the presence of salts.

Amino Acid Sequence↗
PubMed2002

Bacteriocin production by Enterococcus faecium RZS C5 is cell density limited and occurs in the very early growth phase.

Enterocins, bacteriocins produced by enterococci, are gaining interest because of their antilisterial activity. Enterococcus faecium RZS C5, a natural isolate from cheese, produces such a bacteriocin. Generally, bacteriocin production by lactic acid bacteria is a growth-associated process which ceases when cell growth starts to level off. Remarkably, enterocin production by Ent. faecium RZS C5 seems to be limited to the very early growth phase and is switched off at a well-defined cell density of 0.4 g cell dry mass (CDM) l(-1). However, at pH values higher than 6.5, enterocin production displays distinct kinetics. At such pH values, enterocin production is reduced but is maintained until the end of the active growth phase. The relation with cell concentration suggests that enterocin production is part of a severely regulated mechanism. A kinetic model is set up for the description of the early enterocin activity peak. Furthermore, the influence of pH and temperature on the kinetics of growth and bacteriocin production of Ent. faecium RZS C5 was investigated. At pH 6.5, high enterocin activity was obtained in the temperature range 20-35 degrees C. At 35 degrees C, enterocin activity could only be detected between pH 5.5 and 8.0.

Animals↗
PubMed2003

Heterologous production of bacteriocins by lactic acid bacteria.

Over the last two decades, bacteriocins produced by lactic acid bacteria (LAB) have been the subject of considerable research and industrial interest due to their potential as food biopreservatives. The development of heterologous expression systems for such antimicrobial compounds may offer a number of advantages over native systems, such as facilitating the control of bacteriocin gene expression or achieving higher production levels. In addition, the heterologous production by food-grade LAB offers an attractive method for overcoming some of the adverse situations that may affect the effectiveness of some bacteriocins in food systems. Construction of multibacteriocinogenic strains or acquisition of antimicrobial properties by industrial strains are further objectives that can be achieved through the use of heterologous gene expression systems. The development of new biotechnological tools and recent advances in LAB genetics account for the escalating number of studies dealing with heterologous production of bacteriocins by such hosts. This paper reviews the literature published on the subject and compares the different experimental strategies that have been used up to the present for this purpose.

Bacteriocins↗
PubMed2003

Modelling growth and bacteriocin production by Lactobacillus curvatus LTH 1174 in response to temperature and pH values used for European sausage fermentation processes.

Lactobacillus curvatus LTH 1174, a strain isolated from fermented sausage, produces the antilisterial bacteriocin curvacin A. Its biokinetics of cell growth and bacteriocin production as a function of temperature (20-38 degrees C) and pH (4.8-7.0) were investigated in vitro during laboratory fermentations using de Man, Rogosa and Sharpe (MRS) medium. A predictive, successfully validated model was set up to describe the influence of temperature and pH on the microbial behavior. Both cell growth and bacteriocin activity were influenced by changes in temperature and pH. The optimum temperature value for cell growth, 34.5 degrees C, did not correspond with the optimum temperature for curvacin A production (20-27 degrees C). Interestingly, the pH range for growth and curvacin A production was broad. Thus, Lb. curvatus LTH 1174 seems to be a promising bacteriocin-producing strain for use in European sausage fermentations that are performed at temperatures near 25 degrees C.

Animals↗
PubMed1998

Characterization of a bacteriocin produced by Streptococcus thermophilus 81.

A new bacteriocin, produced by Streptococcus thermophilus 81 has been isolated, purified and characterized. By its heat sensitivity and broad inhibitory spectrum it does not resemble any other S. thermophilus bacteriocin. The mode of action is bacteriostatic. This peptide of 32 amino acids is efficient against several Bacillus species, Listeria monocytogenes, Salmonella typhimurium, Escherichia coli, Yersinia pseudotuberculosis and Yersinia enterocolitica. This bacteriocin is heat labile but its activity was not altered by pH variation from 3 to 10. Six months of storage at 40 degrees C did not influence the activity. The inactivation by detergents and the inability to resolve the protein in SDS-PAGE supposes a more complex structure or a possible stabilizing effect of other molecules. The low sensitivity of Lactobacillus delbrueckii subsp. bulgaricus to the isolated bacteriocin suggests that S. thermophilus 81 may be used in yoghurt starters.

Animals↗
PubMed2002

Optimization of a cultural medium for bacteriocin production by Lactococcus lactis using response surface methodology.

The medium composition for bacteriocin production by Lactococcus lactis ATCC 11454 was optimized using response surface methodology. The selected six factors based on CM medium were sucrose, soybean peptone, yeast extract, KH(2)PO(4), NaCl, and MgSO(4).7H(2)O. Fractional factorial designs (FFD) and the path of steepest ascent were effective in searching for the main factors and approaching the optimum region of the response. By a 2(6-2) FFD, sucrose, soybean peptone, yeast extract, KH(2)PO(4) were found to be significant factors and had positive effects on cell growth, however, only soybean peptone and KH(2)PO(4) were shown to be the two significant factors for bacteriocin production and had negative and positive effects, respectively. The effects of the two main factors on bacteriocin production were further investigated by a central composite design and the optimum composition was found to be 1% sucrose, 0.45% soybean peptone, 1% yeast extract, 2.84% KH(2)PO(4), 0.2% NaCl, and 0.02% MgSO(4) x 7H(2)O. The optimal medium allowed bacteriocin yield to be doubled compared to CM medium.

Bacteriocins↗
PubMedDate not supplied

Two-peptide bacteriocins produced by lactic acid bacteria.

Bacteriocins from lactic acid bacteria are ribosomally produced peptides (usually 30-60 amino acids) that display potent antimicrobial activity against certain other Gram-positive organisms. They function by disruption of the membrane of their targets, mediated in at least some cases by interaction of the peptide with a chiral receptor molecule (e.g., lipid II or sugar PTS proteins). Some bacteriocins are unmodified (except for disulfide bridges), whereas others (i.e. lantibiotics) possess extensive post-translational modifications which include multiple monosulfide (lanthionine) bridges and dehydro amino acids as well as possible keto amide residues at the N-terminus. Most known bacteriocins are biologically active as single peptides. However, there is a growing class of two peptide systems, both unmodified and lantibiotic, which are fully active only when both partners are present (usually 1:1). In some cases, neither peptide has activity by itself, whereas in others, the activity of one is enhanced by the other. This review discusses the classification, structure, production, regulation, biological activity, and potential applications of such two-peptide bacteriocins.

Amino Acid Sequence↗
PubMed2003

Purification of bacteriocin AS-48 from an Enterococcus faecium strain and analysis of the gene cluster involved in its production.

The cyclic bacteriocin AS-48 has previously been shown to be produced by Enterococcus faecalis strains. A bacteriocin has been purified from an E. faecium strain (E. faecium 7C5), and it has been found to possess molecular mass, cyclization and amino acid sequence typical of bacteriocin AS-48. In addition to the structural gene as-48A, the sequence analysis of the AS-48 gene cluster present in E. faecium 7C5 has revealed the presence of several putative coding regions presumably involved in bacteriocin production and immunity. The results of DNA hybridization assays have indicated that the AS-48 gene cluster and the gene pd78 are present on the same plasmid, possibly the pPD1 plasmid, in E. faecium 7C5.

Amino Acid Sequence↗
PubMed2002

Phenotypic and genetic characterisation of bacteriocin-producing strains of Staphylococcus aureus involved in bovine mastitis.

Fifty strains of Staphylococcus spp. isolated from bovine mastitis cases in several herds from different Argentinian provinces were screened for antimicrobial substances. Twelve strains exhibited a high antagonistic activity against the indicator strain (Corynebacterium fimi) and were chosen for further characterisation. The antimicrobial substances were sensitive to proteolytic enzymes suggesting that they might be bacteriocins (Bac). These strains were identified as S. aureus by the amplification of the femA gene. Plasmid profile analysis of these strains revealed the presence of at least one plasmid. Eleven strains carried a plasmid with a size similar to that of pRJ6 (8.0kb), which encodes aureocin A70, a bacteriocin produced by the Brazilian S. aureus strain A70 isolated from commercial milk. The other strain harboured a much larger plasmid. PCR experiments, using specific primers for amplification of the bacteriocin operon found in pRJ6, showed that all strains had the expected 525bp amplicon, suggesting that the bacteriocin produced may be related to aureocin A70. The genomic DNA of all Bac(+) strains was then analysed by pulsed-field gel electrophoresis (PFGE) in order to investigate clonal relationships amongst strains. Based on the results of PFGE experiments, 10 out of the 12 Bac(+) strains belonged to the same clone. The remaining two strains are possibly related to the prevalent clone. The aureocin A70 producer-strain belonged to a distinct clone.

Animals↗
PubMed1991

Bacteriocin typing and biotyping of clinical isolates of Serratia marcescens.

A total of 727 clinical isolates of Serratia marcescens from 474 patients were typed for bacteriocin susceptibility; 707 of the isolates (97.25%) were typable and comprised 46 different bacteriocin types. The biotyping method of Grimont and Grimont permitted categorization of 726 of the 727 isolates into 50 biotype profiles. However, 98 of the 726 biotypable isolates (13.5%) yielded previously unknown biotype profiles; similarly, 24 out of 59 reference strains of S. marcescens gave biotype profiles that had not been encountered before. Multiple S. marcescens isolates (366 of the 727 isolates) had been recovered from 113 patients. Phenotypic variation in bacteriocin susceptibility occurred in 15 of these patients, whereas phenotypic variation in biotype profiles was noted in 26 of these patients. In 5 of the 113 patients, phenotypic variation accounted for changes both in bacteriocin type and in biotype profile. It is suggested that serotyping should remain the method of choice until new methods have been evaluated accordingly.

Bacterial Typing Techniques↗
PubMed1996

Bacteriocins: nature, function and structure.

Bacteriocins are extracellular substances produced by different types of bacteria, including both Gram positive and Gram negative species. They can be produced spontaneously or induced by certain chemicals such as mitomycin C. They are biologically one of the important substances, and have been found to be useful in membrane studies and also in typing pathogenic microorganisms causing serious nosocomial infections. Bacteriocins are a heterogeneous group of particles with different morphological and biochemical entities. They range from a simple protein to a high molecular weight complex: the active moiety of each molecule in all cases seems to be protein in nature. The genetic determinants of most of the bacteriocins are located on the plasmids, apart from few which are chromosomally encoded. These bactericidal particles are species specific. They exert their lethal activity through adsorption to specific receptors located on the external surface of sensitive bacteria, followed by metabolic, biological and morphological changes resulting in the killing of such bacteria. This review summarises the classification, biochemical nature, morphology and mode of action of bacteriocins as well as their genetic determinants and the microbiological relevance of these bactericidal agents.

Bacteria↗
PubMed1983

Comparison of different methods for bacteriocin typing of Klebsiella strains.

Epidemiological analysis of Klebsiella strains from nosocomial infections needs a simple, stable and reproducible technique of typing. We have evaluated three bacteriocin typing methods for Klebsiella spp. by means of 15 bacteriocin-producing strains, with special reference to stability and reproducibility. With the three methods indicator strains and clinical strains were retyped on different days under constant test procedures. Stability of bacteriocins was tested by titration immediately after preparation and after 4 weeks of storage at -70 degrees C. Thereafter, reproducibility of typing was tested by means of these freshly prepared bacteriocin lysates and of portions of the same lysates stored at -70 degrees C. A moderate reproducibility was obtained with one method after two typing experiments: 79.2% and 61.3% for indicator strains and clinical strains respectively. The other two methods gave a much lower reproducibility of 38.5% and 32.5% for indicator strains and of 11.1% and 25.5% for clinical strains after two experiments. The reproducibility decreased after retyping three, four or five times. These methods are simple to perform but their usefulness for epidemiological studies is doubtful. Possible causes of the lack of reproducibility of the methods are discussed.

Bacteriocins↗
PubMed1984

A bacteriocin produced by certain M-type 49 Streptococcus pyogenes strains when incubated anaerobically.

Bacteriocin production (P)-typing of 75 M-type 49 group-A streptococci obtained from a variety of epidemiological incidents in different countries gave no evidence of production under the usual aerobic test conditions. However, with anaerobic incubation, 28% of the strains gave a pattern of inhibitory activity against the indicator strains which was indistinguishable from that previously attributed to the bacteriocin, streptococcin A-FF22 (SA-FF22). Isolation and partial purification of the M type 49 bacteriocin (SA-M49) by freeze-thaw elution from anaerobically grown lawn cultures, followed by ammonium sulphate precipitation and Sephadex chromatography, showed the activity to be associated with a heat-stable proteinaceous molecule of molecular weight approximately 8000 - properties similar to those of SA-FF22. SA-FF22 and SA-M49 were found to have identical inhibitory spectra including immunity of the producer strains to the inhibitory activity of both the homologous and heterologous bacteriocin preparations. SA-M49 production occurred in some strains of phage subtypes II, III and provisional VI and, since it was a consistent property for all isolates from single outbreaks of infection, it provides a means of discriminating between strains of each of these three phage subtypes. There was no evidence of any increased incidence of SA-M49 production in M-type 49 strains associated with nephritic sequelae.

Anaerobiosis↗